TFTD_BURCE
ID TFTD_BURCE Reviewed; 515 AA.
AC O87009;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=FADH(2)-dependent monooxygenase TftD;
DE EC=1.14.14.-;
DE AltName: Full=Chlorophenol-4-monooxygenase component 2;
DE AltName: Full=Two component enzyme D;
GN Name=tftD;
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AC1100;
RX PubMed=9603818; DOI=10.1128/aem.64.6.2086-2093.1998;
RA Hubner A., Danganan C.E., Xun L., Chakrabarty A.M., Hendrickson W.;
RT "Genes for 2,4,5-trichlorophenoxyacetic acid metabolism in Burkholderia
RT cepacia AC1100: characterization of the tftC and tftD genes and locations
RT of the tft operons on multiple replicons.";
RL Appl. Environ. Microbiol. 64:2086-2093(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AC1100;
RX PubMed=12700257; DOI=10.1128/jb.185.9.2786-2792.2003;
RA Gisi M.R., Xun L.;
RT "Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin
RT adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia
RT AC1100.";
RL J. Bacteriol. 185:2786-2792(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-289.
RX PubMed=19915006; DOI=10.1074/jbc.m109.056135;
RA Webb B.N., Ballinger J.W., Kim E., Belchik S.M., Lam K.S., Youn B.,
RA Nissen M.S., Xun L., Kang C.;
RT "Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD
RT oxidoreductase (TftC) of Burkholderia cepacia AC1100.";
RL J. Biol. Chem. 285:2014-2027(2010).
CC -!- FUNCTION: Oxygenase component of a two-component system that degrades
CC 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-
CC trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is
CC chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then,
CC TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone.
CC {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35.8 uM for 2,4,5-trichlorophenol {ECO:0000269|PubMed:12700257,
CC ECO:0000269|PubMed:19915006};
CC KM=39.9 uM for 2,4,6-trichlorophenol {ECO:0000269|PubMed:12700257,
CC ECO:0000269|PubMed:19915006};
CC KM=4.3 uM for 2,5-dichloro-p-hydroquinone
CC {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
CC Note=kcat is 0.67 sec(-1) with 2,4,5-trichlorophenol as substrate.
CC kcat is 0.41 sec(-1) with 2,4,6-trichlorophenol as substrate. kcat is
CC 0.1 sec(-1) with 2,5-dichloro-p-hydroquinone as substrate.;
CC -!- PATHWAY: Xenobiotic degradation.
CC -!- SUBUNIT: Homotetramer. The chlorophenol-4-monooxygenase is composed of
CC an oxygenase component TftD and a reductase component TftC.
CC {ECO:0000269|PubMed:19915006}.
CC -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; U83405; AAC23548.2; -; Genomic_DNA.
DR PDB; 3HWC; X-ray; 2.50 A; A/B/C/D=1-515.
DR PDBsum; 3HWC; -.
DR AlphaFoldDB; O87009; -.
DR SMR; O87009; -.
DR KEGG; ag:AAC23548; -.
DR BioCyc; MetaCyc:MON-14674; -.
DR SABIO-RK; O87009; -.
DR EvolutionaryTrace; O87009; -.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR PANTHER; PTHR36117; PTHR36117; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Monooxygenase; Oxidoreductase.
FT CHAIN 1..515
FT /note="FADH(2)-dependent monooxygenase TftD"
FT /id="PRO_0000418743"
FT BINDING 100..104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151..153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 157..160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 203..204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 457..460
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MUTAGEN 289
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19915006"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 179..193
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 253..264
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 280..314
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 320..345
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 359..384
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 394..398
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 434..441
FT /evidence="ECO:0007829|PDB:3HWC"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 449..453
FT /evidence="ECO:0007829|PDB:3HWC"
FT TURN 455..460
FT /evidence="ECO:0007829|PDB:3HWC"
FT HELIX 470..477
FT /evidence="ECO:0007829|PDB:3HWC"
SQ SEQUENCE 515 AA; 57452 MW; CC3281C3E5D9E536 CRC64;
MRTGKQYLES LNDGRVVWVG NEKIDNVATH PLTRDYAERV AQFYDLHHRP DLQDVLTFVD
ADGVRRSRQW QDPKDAAGLR VKRKYHETIL REIAAGSYGR LPDAHNYTFT TYADDPEVWE
KQSIGAEGRN LTQNIHNFLK LLREKDLNCP LNFVDPQTDR SSDAAQARSP NLRIVEKTDD
GIIVNGVKAV GTGIAFGDYM HIGCLYRPGI PGEQVIFAAI PTNTPGVTVF CRESTVKNDP
AEHPLASQGD ELDSTTVFDN VFIPWEQVFH IGNPEHAKLY PQRIFDWVHY HILIRQVLRA
ELIVGLAILI TEHIGTSKLP TVSARVAKLV AFHLAMQAHL IASEETGFHT KGGRYKPNPL
IYDFGRAHFL QNQMSVMYEL LDLAGRSSLM IPSEGQWDDS QSGQWFVKLN NGPKGNPRER
VQIGRVIRDL YLTDWGGRQF MFENFNGTPL FAVFAATMTR DDMSAAGTYG KFASQVCGIE
FGGAEPTAYA ATADYAKALD KGLAPEPAAA ESATS
